E3 Ubiquitin Ligases RNF20 and RNF40 Are Required for Double-Stranded Break (DSB) Repair: Evidence for Monoubiquitination of Histone H2B Lysine 120 as a Novel Axis of DSB Signaling and Repair
Author(s) -
Clare C. So,
Shaliny Ramachandran,
Alberto Martín
Publication year - 2019
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.00488-18
Subject(s) - biology , histone h2b , h3k4me3 , microbiology and biotechnology , ubiquitin , dna repair , histone , non homologous end joining , homologous recombination , ubiquitin ligase , dna damage , sumo protein , dna , genetics , gene , promoter , gene expression
Histone posttranslational modifications play fundamental roles in the regulation of double-stranded DNA break (DSB) repair. RNF20/RNF40-mediated monoubiquitination of histone H2B on lysine 120 (H2Bub) has been suggested as a potential mediator of DSB repair, although the nature and function of this posttranslational modification remain enigmatic.
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